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5cri

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Wild-type Bacillus subtilis lipase A with 0% [BMIM][Cl]

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Retrieved from "http://52.214.119.220/wiki/index.php/5cri"

@@ Line 3: / Line 3: @@
 <StructureSection load='5cri' size='340' side='right'caption='[[5cri]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5cri]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CRI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CRI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5cri]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CRI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CRI FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.63&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lipA, QX56_01625 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5cri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cri OCA], [https://pdbe.org/5cri PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cri RCSB], [https://www.ebi.ac.uk/pdbsum/5cri PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cri ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5cri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cri OCA], [http://pdbe.org/5cri PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cri RCSB], [http://www.ebi.ac.uk/pdbsum/5cri PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cri ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/ESTA_BACSU ESTA_BACSU] Active toward p-nitrophenyl esters and triacylglycerides with a marked preference for esters with C8 acyl groups.<ref>PMID:8396026</ref>
-We present the first crystallographic insight into the interactions of an ionic liquid (IL) with an enzyme, which has widespread implications for stabilizing enzymes in IL media for biocatalysis. Structures of Bacillus subtilis lipase A (lipA) and an IL-stable variant (QM-lipA) were obtained in the presence of increasing concentrations of 1-butyl-3-methylimidazolium chloride ([BMIM][Cl]). These studies revealed that the [BMIM] cation interacts with surface residues through hydrophobic and cation-pi interactions. Of specific interest was the disruption of internal stacking interactions of aromatic side chains by [BMIM], which provides structural evidence for the mechanism of enzyme denaturation by ILs. The interaction of [BMIM] and Cl ions with lipA was reduced by the stabilizing mutations Y49E and G158E in QM-lipA. Ultimately, these findings present the molecular basis for stabilizing enzymes from IL-induced inactivation, as well as the selection of ILs that are less denaturing.
-Crystallographic Investigation of Imidazolium Ionic Liquid Effects on Enzyme Structure.,Nordwald EM, Plaks JG, Snell JR, Sousa MC, Kaar JL Chembiochem. 2015 Nov;16(17):2456-9. doi: 10.1002/cbic.201500398. Epub 2015 Oct, 14. PMID:26388426<ref>PMID:26388426</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5cri" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 25: / Line 17: @@
 __TOC__
 </StructureSection>
-[[Category: Vibrio subtilis ehrenberg 1835]]
+[[Category: Bacillus subtilis]]
 [[Category: Large Structures]]
-[[Category: Triacylglycerol lipase]]
+[[Category: Kaar JL]]
-[[Category: Kaar, J L]]
+[[Category: Nordwald EM]]
-[[Category: Nordwald, E M]]
+[[Category: Plaks JG]]
-[[Category: Plaks, J G]]
+[[Category: Snell JR]]
-[[Category: Snell, J R]]
+[[Category: Sousa MC]]
-[[Category: Sousa, M C]]
-[[Category: Hydrolase]]
-[[Category: Wild-type]]

5cri

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Wild-type Bacillus subtilis lipase A with 0% [BMIM][Cl]

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